Information on EC 2.7.7.58 - (2,3-dihydroxybenzoyl)adenylate synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.7.58
-
RECOMMENDED NAME
GeneOntology No.
(2,3-dihydroxybenzoyl)adenylate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 2,3-dihydroxybenzoate = diphosphate + (2,3-dihydroxybenzoyl)adenylate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of siderophore group nonribosomal peptides
-
-
enterobactin biosynthesis
-
-
NIL
-
-
vibriobactin biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:2,3-dihydroxybenzoate adenylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
122332-73-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
JM109
-
-
Manually annotated by BRENDA team
serotype 01, strain MVM425
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2,3,4-trihydroxybenzoic acid
diphosphate + (2,3,4-trihydroxybenzoyl)adenylate
show the reaction diagram
-
-
-
-
?
ATP + 2,3-dihydroxybenzoate
diphosphate + (2,3-dihydroxybenzoyl)adenylate
show the reaction diagram
ATP + 2,3-dihydroxybenzoate
diphosphate + 2,3-dihydroxybenzoyl adenylate
show the reaction diagram
-
-
-
-
?
ATP + 2,4-dihydroxybenzoic acid
diphosphate + (2,4-dihydroxybenzoyl)adenylate
show the reaction diagram
-
-
-
-
?
ATP + 2,5-dihydroxybenzoic acid
diphosphate + (2,5-dihydroxybenzoyl)adenylate
show the reaction diagram
-
i.e. gentisic acid
-
-
?
ATP + 2-hydroxybenzoic acid
diphosphate + (2-hydroxybenzoyl)adenylate
show the reaction diagram
-
i.e. salicylic acid, not 3- or 4-derivative
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 2,3-dihydroxybenzoate
diphosphate + (2,3-dihydroxybenzoyl)adenylate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-dihydroxybenzohydroxamoyl adenylate
-
strong product analog inhibitor, competitive inhibitor
2-hydroxybenzohydroxamoyl adenylate
-
deletion of the catecholic 3-OH group of 2,3-dihydroxybenzohydroxamoyl adenylate reduces inhibitory activity by a factor of 3.5
acetohydroxamoyl adenylate
-
replacing the entire catechol moiety of 2,3-dihydroxybenzohydroxamoyl adenylate by a hydrogen atom gives up to 10% inhibition
benzohydroxamoyl adenylate
-
deletion of both the catecholic 3-OH and 2-OH group of 2,3-dihydroxybenzohydroxamoyl adenylate reduces inhibitory activity by a factor of 2000
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.093
2,3,4-trihydroxybenzoic acid
-
pH 9.0, 37°C
0.0027
2,3-Dihydroxybenzoic acid
-
pH 9.0, 37°C
0.242
2,4-dihydroxybenzoic acid
-
pH 9.0, 37°C
0.552
2,5-dihydroxybenzoic acid
-
pH 9.0, 37°C
0.091
2-hydroxybenzoic acid
-
pH 9.0, 37°C
1.12
ATP
-
pH 9.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.45
2,3,4-Trihydroxybenzoate
Escherichia coli
-
pH 9.0, 37°C
5.5
2,3-Dihydroxybenzoate
Escherichia coli
-
pH 9.0, 37°C
3.23
2,4-Dihydroxybenzoate
Escherichia coli
-
pH 9.0, 37°C
3.15
2,5-dihydroxybenzoic acid
Escherichia coli
-
pH 9.0, 37°C
2.5
2-hydroxybenzoic acid
Escherichia coli
-
pH 9.0, 37°C
5.83
ATP
Escherichia coli
-
pH 9.0, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000009
2,3-dihydroxybenzohydroxamoyl adenylate
-
product analog inhibitor, competitive inhibitor, result indicates that the catecholic 2-OH group is critical for tight binding
0.000037
2-hydroxybenzohydroxamoyl adenylate
-
product analog inhibitor, competitive inhibitor
1
acetohydroxamoyl adenylate
-
value above 1
0.013
benzohydroxamoyl adenylate
-
product analog inhibitor, competitive inhibitor
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0054
-
specific activity of mutant R437D/K473D by using complete reaction, measuring AMP production with coupled assay
0.018
-
specific activity of mutant R437D by using complete reaction, measuring AMP production with coupled assay
0.156
-
specific activity of mutant K473D by using complete reaction, measuring AMP production with coupled assay
0.165
-
specific activity of mutant R494D by using complete reaction, measuring AMP production with coupled assay
0.18
-
specific activity of wild-type EntE by using complete reaction, measuring AMP production with coupled assay
8.33
-
partially purified enzyme
176.4
-
specific activity of mutant R437D/K473D by measuring diphosphate exchange
182.7
-
specific activity of mutant K473D by measuring diphosphate exchange
189
-
specific activity of mutant R494D by measuring diphosphate exchange
197.4
-
specific activity of mutant R437D by measuring diphosphate exchange
210
-
specific activity of wild-type EntE by measuring diphosphate exchange
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59000
-
2 * 59000, SDS-PAGE
59299
-
x * 59299, DNA sequence determination
60124
x * 60124, calculated, x * 60000, SDS-PAGE
60900
-
x * 60900, calculated from the deduced amino acid sequence
66000
-
dynamic light scattering
115000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 59000, SDS-PAGE
monomer
-
1 * 60000, calculated
additional information
-
dihydro-2,3-dihydroxybenzoate dehydrogenase EntA can form a specific complex with 2,3-dihydroxybenzoate-AMP ligaseEntE with a stoichiometry of one EntA tetramer and four EntE monomers. EntA-EntE binding behavior is sigmoidal
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.3 A resolution, space group P21
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol, 50%, stabilizes dilute enzyme solutions
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C to 2°C, 25 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, 10 mM MgCl2, 50% glycerol, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein is purified by metal chelate chromatography
-
recombinant protein using His-tag with poor purification results, purification by conventional purification methods
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli BL21
-
expressed as His-tag fusion protein in Escherichia coli origami(DE3), complementation of an enzyme deficient Escherichia coli strain
-
expression in Escherichia coli
overexpression in Escherichia coli JM105; structural gene entE subcloned into multi-copy plasmid pKK223-3 under control of tac-promoter, DNA sequence determination
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K473D
-
specific activity of mutant K473D by measuring AMP production with coupled assay= 0.0156 micromol/min/mg, by measuring diphosphate exchange= 182.7 micromol/min/mg
R437D
-
specific activity of mutant R437D by measuring AMP production with coupled assay= 0.018 micromol/min/mg, by measuring diphosphate exchange= 197.4 micromol/min/mg
R437D/K473D
-
specific activity of mutant R437D/K473D by measuring AMP production with coupled assay= 0.0054 micromol/min/mg, by measuring diphosphate exchange= 176.4 micromol/min/mg
R494D
-
specific activity of mutant R494D by measuring AMP production with coupled assay= 0.0165 micromol/min/mg, by measuring diphosphate exchange= 189 micromol/min/mg
additional information
-
mutagenesis studies support hypothesis that members of adenylate -forming family of enzymes adopt two distinct conformations to catalyze the two-step mechanism
Show AA Sequence (961 entries)
Please use the Sequence Search for a specific query.